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LongText Report for: 6i8h-pdb

Name Class
6i8h-pdb
HEADER    IMMUNE SYSTEM                           20-NOV-18   6I8H              
TITLE     STRUCTURE OF THE PLANT IMMUNE SIGNALING NODE EDS1 (ENHANCED DISEASE   
TITLE    2 SUSCEPTIBILITY 1) IN COMPLEX WITH NANOBODY ENB15                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN EDS1L;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1-LIKE;                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EDS1-SPECIFIC NANOBODY;                                    
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: EDS1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  10 ORGANISM_COMMON: LLAMA;                                              
SOURCE  11 ORGANISM_TAXID: 9844;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENHANCED DISEASE SUSCEPTIBILITY 1, PLANT INNATE IMMUNE SYSTEM,        
KEYWDS   2 ALPHA/BETA HYDROLASE FOLD, NANOBODY, IMMUNE SYSTEM                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.NIEFIND,M.VOSS,C.TOELZER                                            
REVDAT   1   02-OCT-19 6I8H    0                                                
JRNL        AUTH   M.VOSS,C.TOELZER,D.D.BHANDARI,J.E.PARKER,K.NIEFIND           
JRNL        TITL   ARABIDOPSIS IMMUNITY REGULATOR EDS1 IN A PAD4/SAG101-UNBOUND 
JRNL        TITL 2 FORM IS A MONOMER WITH AN INHERENTLY INACTIVE CONFORMATION.  
JRNL        REF    J.STRUCT.BIOL.                             2019              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   31550533                                                     
JRNL        DOI    10.1016/J.JSB.2019.09.007                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,E.BRUNSTEIN,J.BAUTOR, 
REMARK   1  AUTH 2 K.NIEFIND,J.E.PARKER                                         
REMARK   1  TITL   STRUCTURAL BASIS FOR SIGNALING BY EXCLUSIVE EDS1 HETEROMERIC 
REMARK   1  TITL 2 COMPLEXES WITH SAG101 OR PAD4 IN PLANT INNATE IMMUNITY.      
REMARK   1  REF    CELL HOST MICROBE             V.  14   619 2013              
REMARK   1  REFN                   ESSN 1934-6069                               
REMARK   1  PMID   24331460                                                     
REMARK   1  DOI    10.1016/J.CHOM.2013.11.006                                   
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.WAGNER,S.RIETZ,J.E.PARKER,K.NIEFIND                        
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF 
REMARK   1  TITL 2 ARABIDOPSIS THALIANA EDS1, A KEY COMPONENT OF PLANT          
REMARK   1  TITL 3 IMMUNITY, IN COMPLEX WITH ITS SIGNALLING PARTNER SAG101.     
REMARK   1  REF    ACTA CRYSTALLOGR. SECT. F     V.  67   245 2011              
REMARK   1  REF  2 STRUCT. BIOL. CRYST. COMMUN.                                 
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   21301097                                                     
REMARK   1  DOI    10.1107/S1744309110051249                                    
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   S.RIETZ,A.STAMM,S.MALONEK,S.WAGNER,D.BECKER,                 
REMARK   1  AUTH 2 N.MEDINA-ESCOBAR,A.C.VLOT,B.J.FEYS,K.NIEFIND,J.E.PARKER      
REMARK   1  TITL   DIFFERENT ROLES OF ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1)   
REMARK   1  TITL 2 BOUND TO AND DISSOCIATED FROM PHYTOALEXIN DEFICIENT4 (PAD4)  
REMARK   1  TITL 3 IN ARABIDOPSIS IMMUNITY.                                     
REMARK   1  REF    NEW PHYTOL.                   V. 191   107 2011              
REMARK   1  REFN                   ISSN 1469-8137                               
REMARK   1  PMID   21434927                                                     
REMARK   1  DOI    10.1111/J.1469-8137.2011.03675.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 8238                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 800                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 72.9578 -  6.6884    1.00     1755   200  0.1954 0.2405        
REMARK   3     2  6.6884 -  5.3092    1.00     1674   160  0.2860 0.3468        
REMARK   3     3  5.3092 -  4.6382    1.00     1595   200  0.2853 0.3405        
REMARK   3     4  4.6382 -  4.2142    0.97     1566   160  0.2953 0.3133        
REMARK   3     5  4.2142 -  3.9122    0.45      722    80  0.3230 0.3952        
REMARK   3     6  3.9122 -  3.6815    0.07      126     0  0.3890 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6024                                  
REMARK   3   ANGLE     :  0.608           8138                                  
REMARK   3   CHIRALITY :  0.041            869                                  
REMARK   3   PLANARITY :  0.005           1058                                  
REMARK   3   DIHEDRAL  : 11.016           3609                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 139 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   2.7833 -43.3036  11.4332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3089 T22:   1.2245                                     
REMARK   3      T33:   1.5785 T12:   0.3158                                     
REMARK   3      T13:   0.4475 T23:   0.0754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0563 L22:   1.4636                                     
REMARK   3      L33:   1.7069 L12:   1.0235                                     
REMARK   3      L13:  -0.4557 L23:  -1.4619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6002 S12:   0.8802 S13:   2.0997                       
REMARK   3      S21:   0.6159 S22:  -0.0435 S23:   0.1064                       
REMARK   3      S31:  -1.6114 S32:  -0.3547 S33:   0.2178                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 337 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4871 -58.4527  15.0646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8860 T22:   1.6993                                     
REMARK   3      T33:   1.4660 T12:   0.0893                                     
REMARK   3      T13:   0.3090 T23:   0.0759                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1666 L22:   2.2192                                     
REMARK   3      L33:   1.9252 L12:   0.4904                                     
REMARK   3      L13:   0.2479 L23:   0.3196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5280 S12:  -0.6941 S13:   0.3657                       
REMARK   3      S21:   0.8778 S22:  -0.1818 S23:   0.1705                       
REMARK   3      S31:  -0.5185 S32:  -0.3283 S33:   0.2893                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 620 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1205 -60.2724 -17.6158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3752 T22:   1.3848                                     
REMARK   3      T33:   0.8022 T12:  -0.2592                                     
REMARK   3      T13:   0.1281 T23:  -0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4344 L22:   1.6657                                     
REMARK   3      L33:   1.1986 L12:   0.8838                                     
REMARK   3      L13:  -1.7657 L23:  -1.7498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4309 S12:   0.9930 S13:  -0.4790                       
REMARK   3      S21:  -0.7451 S22:   0.3051 S23:  -0.5491                       
REMARK   3      S31:   0.2380 S32:  -0.1722 S33:   0.0084                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 17 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8184 -23.7914 -15.6190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1391 T22:   1.8463                                     
REMARK   3      T33:   2.3750 T12:   0.5876                                     
REMARK   3      T13:  -0.2557 T23:   0.0780                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0153 L22:   0.0061                                     
REMARK   3      L33:   0.0686 L12:  -0.0227                                     
REMARK   3      L13:   0.0139 L23:  -0.0625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2684 S12:   0.5159 S13:  -0.1729                       
REMARK   3      S21:  -0.1278 S22:  -0.2236 S23:  -0.3134                       
REMARK   3      S31:  -0.1189 S32:  -0.2640 S33:   0.0007                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 34 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5245 -27.3914  -6.2592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7416 T22:   1.6041                                     
REMARK   3      T33:   2.4918 T12:   0.4774                                     
REMARK   3      T13:  -0.1606 T23:  -0.1474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2009 L22:   0.1765                                     
REMARK   3      L33:   0.2541 L12:   0.2029                                     
REMARK   3      L13:  -0.1930 L23:  -0.2044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3026 S12:  -0.3527 S13:  -0.1236                       
REMARK   3      S21:  -1.6989 S22:  -0.4263 S23:  -0.9207                       
REMARK   3      S31:  -1.8594 S32:   0.6329 S33:  -0.0040                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 35 THROUGH 44 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9496 -36.8433 -17.4982              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5793 T22:   2.1265                                     
REMARK   3      T33:   2.6931 T12:  -0.1567                                     
REMARK   3      T13:  -0.5150 T23:  -0.7592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0582 L22:   0.0049                                     
REMARK   3      L33:   0.0101 L12:   0.0304                                     
REMARK   3      L13:   0.0323 L23:   0.0085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6072 S12:   0.3946 S13:  -0.1341                       
REMARK   3      S21:   0.5433 S22:   0.3668 S23:  -0.4851                       
REMARK   3      S31:   1.6015 S32:  -1.1922 S33:   0.0003                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 51 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1811 -36.8861 -17.0581              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4044 T22:   1.6245                                     
REMARK   3      T33:   3.1242 T12:  -0.0831                                     
REMARK   3      T13:  -0.2259 T23:   0.5495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0494 L22:   0.1836                                     
REMARK   3      L33:   0.2022 L12:   0.0772                                     
REMARK   3      L13:   0.0562 L23:   0.1417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3702 S12:   0.0989 S13:  -0.0662                       
REMARK   3      S21:  -1.7209 S22:  -0.5614 S23:  -0.4144                       
REMARK   3      S31:   1.1837 S32:  -0.2297 S33:  -0.2117                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 67 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0028 -33.0269 -21.0632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3280 T22:   1.5979                                     
REMARK   3      T33:   2.1138 T12:  -0.4499                                     
REMARK   3      T13:  -0.2260 T23:  -0.1380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1493 L22:   0.8431                                     
REMARK   3      L33:   0.3664 L12:  -0.9910                                     
REMARK   3      L13:   0.1962 L23:  -0.1968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9316 S12:  -0.7947 S13:   0.3078                       
REMARK   3      S21:   0.0823 S22:  -1.0957 S23:  -1.2866                       
REMARK   3      S31:   0.8670 S32:  -0.4771 S33:  -0.0007                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7664 -24.3158 -13.0814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2381 T22:   2.3906                                     
REMARK   3      T33:   2.6895 T12:   0.2984                                     
REMARK   3      T13:  -0.2021 T23:   0.3836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1221 L22:   0.0308                                     
REMARK   3      L33:   0.2530 L12:   0.0493                                     
REMARK   3      L13:  -0.0985 L23:  -0.0854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4512 S12:  -0.4921 S13:  -0.2404                       
REMARK   3      S21:  -0.1879 S22:  -0.3205 S23:  -0.0708                       
REMARK   3      S31:   0.0426 S32:   0.0376 S33:  -1.0373                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 96 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0999 -29.7933 -21.9121              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5510 T22:   2.4600                                     
REMARK   3      T33:   1.5421 T12:   0.0990                                     
REMARK   3      T13:  -0.1399 T23:   0.2064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2611 L22:   0.1334                                     
REMARK   3      L33:   0.2061 L12:  -0.0763                                     
REMARK   3      L13:  -0.2576 L23:   0.0330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.4013 S12:  -0.4646 S13:  -0.6206                       
REMARK   3      S21:   0.2710 S22:  -0.1267 S23:   0.2766                       
REMARK   3      S31:   1.8284 S32:  -0.7425 S33:  -0.0298                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 97 THROUGH 111 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2000 -37.8790  -5.2826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6862 T22:   2.0746                                     
REMARK   3      T33:   2.4886 T12:   0.1954                                     
REMARK   3      T13:   0.4647 T23:   0.6343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7348 L22:   6.6180                                     
REMARK   3      L33:   4.3829 L12:  -1.8570                                     
REMARK   3      L13:  -0.2540 L23:   5.1118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.3414 S12:   0.3727 S13:   0.7270                       
REMARK   3      S21:   0.2923 S22:  -1.7843 S23:   1.6079                       
REMARK   3      S31:   0.5666 S32:  -1.1377 S33:  -1.4405                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 118 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.7561 -26.4931 -22.0896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5313 T22:   1.9742                                     
REMARK   3      T33:   1.7623 T12:   0.2632                                     
REMARK   3      T13:  -0.0679 T23:   0.1411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0258 L22:   0.0120                                     
REMARK   3      L33:   0.1224 L12:   0.0062                                     
REMARK   3      L13:   0.0295 L23:  -0.0335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4880 S12:   0.2154 S13:  -0.2402                       
REMARK   3      S21:   0.5217 S22:   0.1367 S23:  -0.6097                       
REMARK   3      S31:   0.2474 S32:  -0.1182 S33:   0.0004                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6I8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012986.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P13 (MX1)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018,          
REMARK 200                                   AUTOPROC VERSION JAN 26, 2018      
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC VERSION 1.0.5, AIMLESS,   
REMARK 200                                   AIMLESS, STARANISO                 
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8246                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.682                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.361                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : 0.11100                            
REMARK 200   FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.34900                            
REMARK 200  R SYM FOR SHELL            (I) : 1.34900                            
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NFU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION: 12.5 % (V/V)      
REMARK 280  (RS)-2-METHYL-2,4-PENTANEDIOL, 12.5 % (W/V) PEG 1000, 12.5 % (W/    
REMARK 280  V) PEG3350, 0.03 M MAGNESIUM CHLORIDE, 0.03 M CALCIUM CHLORIDE,     
REMARK 280  0.0612 M MES, 0.0388 M IMIDAZOLE, PH 6.5; PROTEIN STOCK SOLUTION:   
REMARK 280  4.1 MG/ML PROTEIN, 50 MM SODIUM CHLORIDE, 1 % (V/V) GLYCEROLE,      
REMARK 280  1 MM DTT, 50 MM HEPES, PH 8.0; DROP COMPOSITION: 150 NL PROTEIN     
REMARK 280  STOCK SOLUTION PLUS 225 NL RESERVOIR SOLUTION; CRYO CONDITIONS:     
REMARK 280  THE CRYSTALS WERE FLASH FROZEN DIRECTLY FROM THE EQUILIBRATED       
REMARK 280  CRYSTALLIZATION DROPS., VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 277.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       76.38500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       76.38500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       76.38500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       76.38500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       76.38500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       76.38500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     THR A   621                                                      
REMARK 465     ASP A   622                                                      
REMARK 465     THR A   623                                                      
REMARK 465     LEU A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     HIS A   626                                                      
REMARK 465     HIS A   627                                                      
REMARK 465     HIS A   628                                                      
REMARK 465     HIS A   629                                                      
REMARK 465     HIS A   630                                                      
REMARK 465     HIS A   631                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ALA B   129                                                      
REMARK 465     ALA B   130                                                      
REMARK 465     ALA B   131                                                      
REMARK 465     TYR B   132                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     TYR B   134                                                      
REMARK 465     ASP B   135                                                      
REMARK 465     VAL B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     TYR B   139                                                      
REMARK 465     GLY B   140                                                      
REMARK 465     SER B   141                                                      
REMARK 465     HIS B   142                                                      
REMARK 465     HIS B   143                                                      
REMARK 465     HIS B   144                                                      
REMARK 465     HIS B   145                                                      
REMARK 465     HIS B   146                                                      
REMARK 465     HIS B   147                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  29      -59.04     61.82                                   
REMARK 500    ASP A  98      119.67    -38.13                                   
REMARK 500    SER A 123     -132.68     57.06                                   
REMARK 500    ASN A 144       78.19   -159.82                                   
REMARK 500    PRO A 145       92.55    -69.67                                   
REMARK 500    VAL A 161      -51.20   -120.29                                   
REMARK 500    SER A 216       35.24    -97.51                                   
REMARK 500    GLN B  14     -160.35    -79.12                                   
REMARK 500    ARG B  28       90.81    -63.75                                   
REMARK 500    THR B  29      -70.27   -100.48                                   
REMARK 500    PHE B  30     -107.28     17.92                                   
REMARK 500    PRO B  46      105.29    -56.01                                   
REMARK 500    ARG B  50       74.15    -63.00                                   
REMARK 500    VAL B  53      -65.38    -93.15                                   
REMARK 500    SER B  57       49.51    -82.32                                   
REMARK 500    SER B  58     -120.62     52.95                                   
REMARK 500    ASP B  69      -85.41     56.52                                   
REMARK 500    LYS B  72      105.66    -40.54                                   
REMARK 500    ARG B  75      -42.50   -137.53                                   
REMARK 500    LEU B 109        9.45     58.74                                   
REMARK 500    ASN B 116       14.38   -157.21                                   
REMARK 500    SER B 127     -149.34   -103.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6I8H A    1   623  UNP    Q9XF23   EDS1L_ARATH      1    623             
DBREF  6I8H B    1   147  PDB    6I8H     6I8H             1    147             
SEQADV 6I8H LEU A  624  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H GLU A  625  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H HIS A  626  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H HIS A  627  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H HIS A  628  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H HIS A  629  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H HIS A  630  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8H HIS A  631  UNP  Q9XF23              EXPRESSION TAG                 
SEQRES   1 A  631  MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU          
SEQRES   2 A  631  ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU          
SEQRES   3 A  631  THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL          
SEQRES   4 A  631  ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE          
SEQRES   5 A  631  PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS          
SEQRES   6 A  631  LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY          
SEQRES   7 A  631  LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS          
SEQRES   8 A  631  ASN LEU GLU ALA VAL ILE ASP PRO ARG THR SER PHE GLN          
SEQRES   9 A  631  ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE          
SEQRES  10 A  631  VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE          
SEQRES  11 A  631  LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG          
SEQRES  12 A  631  ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE          
SEQRES  13 A  631  GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA          
SEQRES  14 A  631  LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE          
SEQRES  15 A  631  VAL THR ARG PHE ASP ILE VAL PRO ARG ILE THR LEU ALA          
SEQRES  16 A  631  ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU          
SEQRES  17 A  631  ALA GLN LEU ASP PRO ARG ASN SER SER VAL GLN GLU SER          
SEQRES  18 A  631  GLU GLN ARG ILE THR GLU PHE TYR THR SER VAL MET ARG          
SEQRES  19 A  631  ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU          
SEQRES  20 A  631  THR GLY SER ALA GLU ALA ILE LEU GLU THR LEU SER SER          
SEQRES  21 A  631  PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE          
SEQRES  22 A  631  VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN          
SEQRES  23 A  631  SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR CYS GLN          
SEQRES  24 A  631  ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG          
SEQRES  25 A  631  SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN          
SEQRES  26 A  631  SER MET GLY MET LYS LEU PHE ASN HIS LEU ASP GLY GLU          
SEQRES  27 A  631  ASN SER ILE GLU SER SER LEU ASN ASP LEU GLY VAL SER          
SEQRES  28 A  631  THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU          
SEQRES  29 A  631  GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN          
SEQRES  30 A  631  VAL ILE GLN GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP          
SEQRES  31 A  631  ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS          
SEQRES  32 A  631  ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU          
SEQRES  33 A  631  ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA          
SEQRES  34 A  631  GLY VAL PHE ASP GLU VAL LEU GLY LEU LEU LYS LYS CYS          
SEQRES  35 A  631  GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE          
SEQRES  36 A  631  LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU          
SEQRES  37 A  631  ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP          
SEQRES  38 A  631  THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR          
SEQRES  39 A  631  ILE TYR ALA GLN ARG GLY TYR GLU HIS HIS ILE LEU LYS          
SEQRES  40 A  631  PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS          
SEQRES  41 A  631  VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE          
SEQRES  42 A  631  GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER          
SEQRES  43 A  631  CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO          
SEQRES  44 A  631  TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY          
SEQRES  45 A  631  MET LEU ARG GLU TRP ILE THR ALA GLY GLU VAL ASP GLU          
SEQRES  46 A  631  LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP          
SEQRES  47 A  631  TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO          
SEQRES  48 A  631  LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR LEU          
SEQRES  49 A  631  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  137  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  137  ALA GLY GLY SER LEU ARG LEU SER CYS ALA GLY SER GLY          
SEQRES   3 B  137  ARG THR PHE SER THR TYR ASP MET ALA TRP PHE ARG GLN          
SEQRES   4 B  137  ALA PRO GLY LYS GLU ARG GLU PHE VAL SER SER ILE SER          
SEQRES   5 B  137  SER SER GLY GLY ASN VAL VAL TYR ARG ASP SER VAL LYS          
SEQRES   6 B  137  GLY ARG PHE THR ILE ALA ARG ASP ASN ALA ALA ASN ALA          
SEQRES   7 B  137  VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR          
SEQRES   8 B  137  ALA VAL TYR TYR CYS ALA ALA LYS TRP LEU ALA ALA ASP          
SEQRES   9 B  137  TYR ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER          
SEQRES  10 B  137  SER ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY          
SEQRES  11 B  137  SER HIS HIS HIS HIS HIS HIS                                  
HELIX    1 AA1 PHE A    3  GLY A    8  1                                   6    
HELIX    2 AA2 ASN A   10  ALA A   24  1                                  15    
HELIX    3 AA3 TYR A   25  THR A   27  5                                   3    
HELIX    4 AA4 SER A   48  PHE A   52  5                                   5    
HELIX    5 AA5 GLU A   87  ASP A   98  1                                  12    
HELIX    6 AA6 PRO A   99  THR A  101  5                                   3    
HELIX    7 AA7 SER A  102  SER A  113  1                                  12    
HELIX    8 AA8 SER A  123  TYR A  140  1                                  18    
HELIX    9 AA9 PHE A  141  ASN A  144  5                                   4    
HELIX   10 AB1 ASP A  163  GLU A  173  1                                  11    
HELIX   11 AB2 TRP A  175  ARG A  177  5                                   3    
HELIX   12 AB3 ILE A  188  ALA A  195  5                                   8    
HELIX   13 AB4 THR A  203  ASP A  212  1                                  10    
HELIX   14 AB5 SER A  221  THR A  248  1                                  28    
HELIX   15 AB6 ALA A  251  LEU A  262  1                                  12    
HELIX   16 AB7 ASN A  286  THR A  297  1                                  12    
HELIX   17 AB8 LEU A  308  ASP A  316  1                                   9    
HELIX   18 AB9 SER A  319  SER A  326  1                                   8    
HELIX   19 AC1 MET A  327  LYS A  330  5                                   4    
HELIX   20 AC2 ASP A  336  GLU A  338  5                                   3    
HELIX   21 AC3 ILE A  341  LEU A  348  1                                   8    
HELIX   22 AC4 SER A  351  GLN A  381  1                                  31    
HELIX   23 AC5 GLN A  381  GLU A  394  1                                  14    
HELIX   24 AC6 GLU A  394  HIS A  402  1                                   9    
HELIX   25 AC7 ASN A  404  SER A  413  1                                  10    
HELIX   26 AC8 GLU A  415  LYS A  441  1                                  27    
HELIX   27 AC9 PRO A  445  GLY A  450  5                                   6    
HELIX   28 AD1 ASP A  451  HIS A  476  1                                  26    
HELIX   29 AD2 LEU A  477  THR A  482  1                                   6    
HELIX   30 AD3 PRO A  484  GLY A  489  1                                   6    
HELIX   31 AD4 PRO A  491  LYS A  507  1                                  17    
HELIX   32 AD5 PRO A  508  GLY A  510  5                                   3    
HELIX   33 AD6 ILE A  512  LEU A  524  1                                  13    
HELIX   34 AD7 GLN A  529  LEU A  537  1                                   9    
HELIX   35 AD8 SER A  540  SER A  546  5                                   7    
HELIX   36 AD9 CYS A  547  LYS A  556  1                                  10    
HELIX   37 AE1 VAL A  563  ALA A  580  1                                  18    
HELIX   38 AE2 ASP A  584  PHE A  589  1                                   6    
HELIX   39 AE3 SER A  593  THR A  601  1                                   9    
HELIX   40 AE4 PRO A  603  HIS A  609  1                                   7    
HELIX   41 AE5 LEU A  612  MET A  616  5                                   5    
HELIX   42 AE6 LYS B   95  THR B   99  5                                   5    
SHEET    1 AA1 8 TYR A  30  ALA A  35  0                                        
SHEET    2 AA1 8 VAL A  38  PHE A  43 -1  O  VAL A  38   N  ALA A  35           
SHEET    3 AA1 8 GLN A 116  HIS A 122  1  O  VAL A 118   N  PHE A  41           
SHEET    4 AA1 8 ARG A 152  PHE A 156  1  O  ARG A 152   N  PHE A 119           
SHEET    5 AA1 8 PHE A 179  THR A 184  1  O  PHE A 182   N  THR A 155           
SHEET    6 AA1 8 THR A 272  SER A 276  1  O  VAL A 274   N  ASN A 181           
SHEET    7 AA1 8 ARG A 280  VAL A 284 -1  O  VAL A 284   N  PHE A 273           
SHEET    8 AA1 8 LEU A 331  HIS A 334  1  O  LEU A 331   N  LEU A 281           
SHEET    1 AA2 2 GLU A  63  LYS A  65  0                                        
SHEET    2 AA2 2 THR A  84  ASN A  86 -1  O  VAL A  85   N  ILE A  64           
SHEET    1 AA3 4 LEU B   4  SER B   7  0                                        
SHEET    2 AA3 4 LEU B  19  GLY B  25 -1  O  ALA B  24   N  GLN B   5           
SHEET    3 AA3 4 ALA B  86  MET B  91 -1  O  MET B  91   N  LEU B  19           
SHEET    4 AA3 4 PHE B  76  ASP B  81 -1  N  ALA B  79   O  TYR B  88           
SHEET    1 AA4 4 ARG B  50  SER B  55  0                                        
SHEET    2 AA4 4 ALA B  40  GLN B  44 -1  N  TRP B  41   O  SER B  54           
SHEET    3 AA4 4 ALA B 100  CYS B 104 -1  O  TYR B 103   N  PHE B  42           
SHEET    4 AA4 4 THR B 122  VAL B 124 -1  O  THR B 122   N  TYR B 102           
SSBOND   1 CYS B   23    CYS B  104                          1555   1555  2.03  
CRYST1  145.887  145.887  152.770  90.00  90.00 120.00 P 63 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006855  0.003958  0.000000        0.00000                         
SCALE2      0.000000  0.007915  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006546        0.00000                         
TER    5012      ILE A 620                                                      
TER    5895      SER B 128                                                      
MASTER      529    0    0   42   18    0    0    6 5893    2    2   60          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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